F1_VACCA
ID F1_VACCA Reviewed; 222 AA.
AC O57173;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 29-SEP-2021, entry version 67.
DE RecName: Full=Protein F1;
GN OrderedLocusNames=MVA029L, ACAM3000_MVA_029;
OS Vaccinia virus (strain Ankara) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=126794;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT "The complete genomic sequence of the modified vaccinia Ankara strain:
RT comparison with other orthopoxviruses.";
RL Virology 244:365-396(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Acambis 3000;
RA Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA Khristova M., Wohlhueter R.M.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, INTERACTION WITH HOST BCL2L11/BIM, MUTAGENESIS OF VAL-100;
RP ILE-125; VAL-129; GLY-140; VAL-141; ALA-144 AND PHE-148, AND X-RAY
RP CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 18-186.
RX PubMed=18551131; DOI=10.1038/cdd.2008.83;
RA Kvansakul M., Yang H., Fairlie W.D., Czabotar P.E., Fischer S.F.,
RA Perugini M.A., Huang D.C., Colman P.M.;
RT "Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped
RT dimer that binds a highly selective subset of BH3-containing death
RT ligands.";
RL Cell Death Differ. 15:1564-1571(2008).
CC -!- FUNCTION: Protein with a BCL2-like fold which is essential for survival
CC of infected cells.
CC -!- SUBUNIT: Homodimer. Interacts with host pro-apoptotic protein BCL2L11
CC (via BH3 domain). {ECO:0000269|PubMed:18551131}.
CC -!- SIMILARITY: Belongs to the poxviridae F1 protein family. {ECO:0000305}.
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DR EMBL; U94848; AAB96412.1; -; Genomic_DNA.
DR EMBL; AY603355; AAT10427.1; -; Genomic_DNA.
DR PIR; T30779; T30779.
DR PDB; 2VTY; X-ray; 2.10 A; A=18-186.
DR PDB; 4D2L; X-ray; 2.90 A; A=18-186.
DR PDB; 4D2M; X-ray; 2.10 A; A/C=18-186.
DR PDBsum; 2VTY; -.
DR PDBsum; 4D2L; -.
DR PDBsum; 4D2M; -.
DR SASBDB; O57173; -.
DR SMR; O57173; -.
DR MEROPS; I91.001; -.
DR EvolutionaryTrace; O57173; -.
DR Proteomes; UP000159908; Genome.
DR Proteomes; UP000172909; Genome.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IEA:UniProtKB-KW.
DR DisProt; DP01539; -.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR011207; Orthopox_F1.
DR InterPro; IPR021119; Poxvirus_F1/C10.
DR Pfam; PF11099; M11L; 1.
DR PIRSF; PIRSF015971; VAC_F1L; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host-virus interaction;
KW Inhibition of host apoptosis by viral BCL2-like protein;
KW Modulation of host cell apoptosis by virus.
FT CHAIN 1..222
FT /note="Protein F1"
FT /id="PRO_0000099472"
FT MUTAGEN 100
FT /note="V->A: Complete loss of binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 100
FT /note="V->F: No effect on the binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 125
FT /note="I->A: Complete loss of binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 125
FT /note="I->A: Increased binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 129
FT /note="V->L: No effect on the binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 140
FT /note="G->F: Complete loss of binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 141
FT /note="V->F: Increased binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 141
FT /note="V->L: No effect on the binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 144
FT /note="A->F: Increased binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT MUTAGEN 148
FT /note="F->A,E: Complete loss of binding to host BCL2L11."
FT /evidence="ECO:0000269|PubMed:18551131"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:2VTY"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:2VTY"
FT HELIX 58..81
FT /evidence="ECO:0007829|PDB:2VTY"
FT HELIX 84..103
FT /evidence="ECO:0007829|PDB:2VTY"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:4D2M"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2VTY"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:2VTY"
FT HELIX 139..155
FT /evidence="ECO:0007829|PDB:2VTY"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:2VTY"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:2VTY"
SQ SEQUENCE 222 AA; 25910 MW; 1454A5A943DD72B4 CRC64;
MLSMFMCNNI VDYVDGIVQD IEDEASNNVD HDYVYPLPEN MVYRFDKSTN ILDYLSTERD
HVMMAVRYYM SKQRLDDLYR QLPTKTRSYI DIINIYCDKV SNDYNRDMNI MYDMASTKSF
TVYDINNEVN TILMDNKGLG VRLATISFIT ELGRRCMNPV KTIKMFTLLS HTICDDCFVD
YITDISPPDN TIPNTSTREY LKLIGITAIM FATYKTLKYM IG
